Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5ZBB

Crystal structure of Rtt109-Asf1-H3-H4 complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004402	molecular_function	histone acetyltransferase activity
A	0005634	cellular_component	nucleus
A	0006325	biological_process	chromatin organization
A	0006338	biological_process	chromatin remodeling
A	0006351	biological_process	DNA-templated transcription
A	0006355	biological_process	regulation of DNA-templated transcription
A	0006974	biological_process	DNA damage response
A	0010484	molecular_function	histone H3 acetyltransferase activity
A	0016740	molecular_function	transferase activity
A	0032931	molecular_function	histone H3K56 acetyltransferase activity
A	0061733	molecular_function	protein-lysine-acetyltransferase activity
B	0005634	cellular_component	nucleus
B	0006325	biological_process	chromatin organization
C	0000776	cellular_component	kinetochore
C	0000786	cellular_component	nucleosome
C	0003677	molecular_function	DNA binding
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005694	cellular_component	chromosome
C	0006325	biological_process	chromatin organization
C	0006355	biological_process	regulation of DNA-templated transcription
C	0006878	biological_process	intracellular copper ion homeostasis
C	0007080	biological_process	mitotic metaphase chromosome alignment
C	0008823	molecular_function	cupric reductase (NADH) activity
C	0009060	biological_process	aerobic respiration
C	0009303	biological_process	rRNA transcription
C	0030527	molecular_function	structural constituent of chromatin
C	0031492	molecular_function	nucleosomal DNA binding
C	0031507	biological_process	heterochromatin formation
C	0042790	biological_process	nucleolar large rRNA transcription by RNA polymerase I
C	0042802	molecular_function	identical protein binding
C	0043505	cellular_component	CENP-A containing nucleosome
C	0043935	biological_process	sexual sporulation resulting in formation of a cellular spore
C	0045943	biological_process	positive regulation of transcription by RNA polymerase I
C	0046982	molecular_function	protein heterodimerization activity
C	0051382	biological_process	kinetochore assembly
C	0070911	biological_process	global genome nucleotide-excision repair
D	0000786	cellular_component	nucleosome
D	0003677	molecular_function	DNA binding
D	0005515	molecular_function	protein binding
D	0005634	cellular_component	nucleus
D	0005694	cellular_component	chromosome
D	0006325	biological_process	chromatin organization
D	0006334	biological_process	nucleosome assembly
D	0006355	biological_process	regulation of DNA-templated transcription
D	0030527	molecular_function	structural constituent of chromatin
D	0042790	biological_process	nucleolar large rRNA transcription by RNA polymerase I
D	0042802	molecular_function	identical protein binding
D	0045943	biological_process	positive regulation of transcription by RNA polymerase I
D	0046982	molecular_function	protein heterodimerization activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	binding site for residue IOD A 601

Chain	Residue
A	TRP168

site_id	AC2
Number of Residues	1
Details	binding site for residue IOD A 604

Chain	Residue
A	LEU296

site_id	AC3
Number of Residues	1
Details	binding site for residue IOD A 606

Chain	Residue
A	GLN242

site_id	AC4
Number of Residues	1
Details	binding site for residue IOD A 608

Chain	Residue
A	SER109

site_id	AC5
Number of Residues	1
Details	binding site for residue IOD A 609

Chain	Residue
A	ARG464

site_id	AC6
Number of Residues	2
Details	binding site for residue IOD A 610

Chain	Residue
A	ARG162
A	GLU215

site_id	AC7
Number of Residues	3
Details	binding site for residue IOD A 611

Chain	Residue
A	ARG170
A	SER109
A	ARG112

site_id	AC8
Number of Residues	2
Details	binding site for residue PEG A 612

Chain	Residue
A	ALA93
A	ASP94

site_id	AC9
Number of Residues	1
Details	binding site for residue IOD B 201

Chain	Residue
B	VAL107

site_id	AD1
Number of Residues	1
Details	binding site for residue IOD C 201

Chain	Residue
C	PHE84

site_id	AD2
Number of Residues	1
Details	binding site for residue IOD C 202

Chain	Residue
C	LYS125

site_id	AD3
Number of Residues	4
Details	binding site for residue IOD C 204

Chain	Residue
C	ARG63
C	ARG63
C	LYS64
C	LYS64

site_id	AD4
Number of Residues	2
Details	binding site for residue IOD C 205

Chain	Residue
C	SER86
C	SER87

site_id	AD5
Number of Residues	3
Details	binding site for residue IOD C 208

Chain	Residue
C	LYS121
D	SER47
D	LEU49

site_id	AD6
Number of Residues	2
Details	binding site for residue IOD D 201

Chain	Residue
C	ARG63
D	THR30

Functional Information from PROSITE/UniProt

site_id	PS00047
Number of Residues	5
Details	HISTONE_H4 Histone H4 signature. GAKRH

Chain	Residue	Details
D	GLY14-HIS18

site_id	PS00322
Number of Residues	7
Details	HISTONE_H3_1 Histone H3 signature 1. KAPRKQL

Chain	Residue	Details
C	LYS14-LEU20

site_id	PS00959
Number of Residues	9
Details	HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI

Chain	Residue	Details
C	PRO66-ILE74

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"N6-propionyllysine; alternate","evidences":[{"source":"PubMed","id":"19113941","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"17194708","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"22389435","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"22389435","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"PubMed","id":"19113941","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17287358","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"16768447","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	1
Details	Modified residue: {"description":"N6-glutaryllysine","evidences":[{"source":"PubMed","id":"31542297","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)